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Heat shock 22kDa protein 8

Hsp22, HspB8, H-11
The protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. The expression of this gene in induced by estrogen in estrogen receptor-positive breast cancer cells, and this protein also functions as a chaperone in association with Bag3, a stimulator of macroautophagy. Thus, this gene appears to be involved in regulation of cell proliferation, apoptosis, and carcinogenesis, and mutations in this gene have been associated with different neuromuscular diseases, including Charcot-Marie-Tooth disease. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, HSP27, HSP70, HAD, BAG3
Papers on Hsp22
Novel SNPs in HSPB8 gene and their association with heat tolerance traits in Sahiwal indigenous cattle.
M R et al., Karnāl, India. In Trop Anim Health Prod, Jan 2016
HSPB8 gene has been mapped on Bos taurus autosome 17 (BTA-17) spanning nearly 13,252 bp and comprising three exons and two introns.
Mutations in HSPB8 causing a new phenotype of distal myopathy and motor neuropathy.
Udd et al., Sydney, Australia. In Neurology, Jan 2016
OBJECTIVE: To report novel disease and pathology due to HSPB8 mutations in 2 families with autosomal dominant distal neuromuscular disease showing both myofibrillar and rimmed vacuolar myopathy together with neurogenic changes.
Expression profiling of heat shock genes in a scuttle fly Megaselia scalaris (Diptera, Phoridae).
Kowalewska et al., Warsaw, Poland. In J Exp Zool A Ecol Genet Physiol, Nov 2015
The first class consists of hsp22 (larvae), hsp23 (larvae), and hsp26 (both larvae and imagoes), and is upregulated at the lowest temperature (33°C).
A Role for the Chaperone Complex BAG3-HSPB8 in Actin Dynamics, Spindle Orientation and Proper Chromosome Segregation during Mitosis.
Lavoie et al., Québec, Canada. In Plos Genet, Oct 2015
The co-chaperone BAG3, in complex with the heat shock protein HSPB8, plays a role in protein quality control during mechanical strain.
Mitochondrial dynamics and inherited peripheral nerve diseases.
Piscosquito et al., Milano, Italy. In Neurosci Lett, Jul 2015
Microtubules, neurofilaments, and chaperones such as heat shock proteins (HSPs) also have a fundamental role in mitochondrial transport and mutations in some of related encoding genes cause peripheral neuropathy (TUBB3, NEFL, HSPB1, HSPB8, HSPB3, DNAJB2).
Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners.
Kampinga et al., Groningen, Netherlands. In Plos One, 2014
Previous studies showed that co-expression of HSPB1 and HSPB8 can prevent the aggregation associated with the HSPB5 (R120G) mutant in cardiomyocytes and in transgenic mice.
Small heat shock proteins are induced during multiple sclerosis lesion development in white but not grey matter.
Amor et al., Amsterdam, Netherlands. In Acta Neuropathol Commun, 2014
We analysed transcript levels and protein distribution profiles for HSPB1, HSPB6, HSPB8 and HSPB11 in MS lesions at different stages, comparing them with normal-appearing brain tissue from MS patients and non-neurological controls.
Aberrant Autophagic Response in The Muscle of A Knock-in Mouse Model of Spinal and Bulbar Muscular Atrophy.
Poletti et al., Milano, Italy. In Sci Rep, 2014
Using SBMA AR113Q mice we analyzed proteotoxic stress-induced alterations of HSPB8-mediated PQC machinery promoting clearance of misfolded proteins by autophagy.
Neuropathy- and myopathy-associated mutations in human small heat shock proteins: Characteristics and evolutionary history of the mutation sites.
Wertheim et al., In Mutat Res Rev Mutat Res, 2014
In HspB1, HspB3, and HspB8 all known mutations cause motor neuropathies, whereas in HspB5 they cause myopathies.
The small heat shock protein HspB8: role in nervous system physiology and pathology.
Negro et al., Padova, Italy. In Cns Neurol Disord Drug Targets, 2013
A recently identified member of the small heat shock protein family, HspB8, is of particular interest in the field of neurological diseases since mutations in its sequence correlate with development of distal hereditary motor neuropathy and Charcot-Marie-Tooth disease.
Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.
Gibert et al., Lyon, France. In Int J Hyperthermia, 2013
AIMS: To understand the functions of the stress-inducible members of the sHSP family, HspB1, HspB5 and HspB8, and be able to therapeutically modulate their activities, researchers are faced with the complex oligomerisation and phosphorylation properties of these proteins and with their ability to interact with each other and with specific protein targets.
Mutations of small heat shock proteins and human congenital diseases.
Gusev et al., Moscow, Russia. In Biochemistry (mosc), 2012
The data on HspB6 and HspB8 mutations are presented, and feasible effects of these mutations on proteins structure are analyzed.
Cardiac H11 kinase/Hsp22 stimulates oxidative phosphorylation and modulates mitochondrial reactive oxygen species production: Involvement of a nitric oxide-dependent mechanism.
Morin et al., Créteil, France. In Free Radic Biol Med, 2012
protection of mitochondrial function during ischemia via NO-sensitive mechanism
NF-κB regulates protein quality control after heat stress through modulation of the BAG3-HspB8 complex.
Kretz-Remy et al., Lyon, France. In J Cell Sci, 2012
findings show that during heat shock recovery NF-kappaB activates selective removal of misfolded or aggregated proteins by controlling expression of BAG3 and HSPB8 and by modulating the level of the BAG3-HspB8 complex
Developmental expression pattern of Hspb8 mRNA in the mouse brain: analysis through online databases.
Marín et al., Murcia, Spain. In Anat Rec (hoboken), 2012
Hspb8 mRNA is constitutively expressed in specific brain structures across ontogeny; eventually these structures could be affected by the malfunction or deregulation of the Hspb8 molecule.
Downregulation of hsp22 gene expression in Drosophila melanogaster from sites located near chemical plants.
Gavrila et al., Bucureşti, Romania. In Genet Mol Res, 2011
hsp22 could play an important role in relation to stress resistance and adaptation.
Restored expression of the atypical heat shock protein H11/HspB8 inhibits the growth of genetically diverse melanoma tumors through activation of novel TAK1-dependent death pathways.
Aurelian et al., Baltimore, United States. In Cell Death Dis, 2011
The expression of HspB8 inhibits the growth of genetically diverse melanoma cells that include caspase-1 activation outside of the realm of the inflammasome, mTORC1-dependent Beclin-1 upregulation and its cleavage by the activated caspase-1.
Large potentials of small heat shock proteins.
Gusev et al., Moscow, Russia. In Physiol Rev, 2011
HSPB8 (HSP22) prevents accumulation of aggregated proteins in the cell and participates in the regulation of proteolysis of unfolded proteins.
Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy.
Timmerman et al., Antwerp, Belgium. In Nat Genet, 2004
In two pedigrees with distal hereditary motor neuropathy type II linked to chromosome 12q24.3, we identified the same mutation (K141N) in small heat-shock 22-kDa protein 8 (encoded by HSPB8; also called HSP22).
Translational and transcriptional control elements in the untranslated leader of the heat-shock gene hsp22.
Gehring et al., In Cell, 1986
Downstream of the transcription start site in the Drosophila heat-shock gene hsp22, we have identified a region that is necessary for efficient transcription, and also for selective translation during heat shock.
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